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Crystal structure of hpxw

Analyse Crystal structure of hpxw in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5HFT
Type
protein
Length
906 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Gamma-glutamyltranspeptidase
UniProt
A6T9C8
Pockets
10 · best druggability 0.61

Structure

x-ray diffraction · 4 distinct chains · 35% helix, 19% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AGamma-glutamyltranspeptidaseprotein30545% helix, 12% strandA6T9C8
CGamma-glutamyltranspeptidaseprotein29844% helix, 13% strandA6T9C8
BGamma-glutamyltranspeptidaseprotein14915% helix, 33% strandA6T9C8
DGamma-glutamyltranspeptidaseprotein15414% helix, 29% strandA6T9C8

Pockets

10 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11280.610.8524empty
22860.590.7937empty
32070.570.8032empty
42030.550.7929empty
52120.530.7747empty

Interfaces

5 interfaces between chains.

  • C–D · 4780 Ų buried · 84 hydrogen bonds · protein-protein
  • A–B · 4606 Ų buried · 77 hydrogen bonds · protein-protein
  • A–C · 814 Ų buried · 12 hydrogen bonds · protein-protein
  • A–D · 312 Ų buried · 2 hydrogen bonds · protein-protein
  • C–B · 304 Ų buried · 2 hydrogen bonds · protein-protein

Compared structures

  • 5HFT · Crystal structure of HpxW · the same entry in another collection · chain D against D, TM-score 1.00
  • A6T9C8 · AlphaFold monomer V2.0 prediction for oxamate amidohydrolase proenzyme (A6T9C8) · a predicted model of the same protein · chain C against A, TM-score 0.94

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